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Volumn 7, Issue 9, 2011, Pages

Envelope deglycosylation enhances antigenicity of hiv-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodies

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN GP 140; HUMAN IMMUNODEFICIENCY VIRUS ANTIGEN; MONOCLONAL ANTIBODY 2F5; MONOCLONAL ANTIBODY 4E10; EPITOPE; GLYCOPEPTIDASE; GLYCOPROTEIN GP 41; GP140 ENVELOPE PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; VIRUS ENVELOPE PROTEIN;

EID: 80053459912     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002200     Document Type: Article
Times cited : (75)

References (61)
  • 1
    • 0028235930 scopus 로고
    • Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS
    • Muster T, Guinea R, Trkola A, Purtscher M, Klima A, et al. (1994) Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS. J Virol 68: 4031-4034.
    • (1994) J Virol , vol.68 , pp. 4031-4034
    • Muster, T.1    Guinea, R.2    Trkola, A.3    Purtscher, M.4    Klima, A.5
  • 2
    • 0034759882 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41
    • Zwick MB, Labrijn AF, Wang M, Spenlehauer C, Saphire EO, et al. (2001) Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J Virol 75: 10892-10905.
    • (2001) J Virol , vol.75 , pp. 10892-10905
    • Zwick, M.B.1    Labrijn, A.F.2    Wang, M.3    Spenlehauer, C.4    Saphire, E.O.5
  • 3
    • 11144227042 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1
    • Zwick MB, Jensen R, Church S, Wang M, Stiegler G, et al. (2005) Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1. J Virol 79: 1252-1261.
    • (2005) J Virol , vol.79 , pp. 1252-1261
    • Zwick, M.B.1    Jensen, R.2    Church, S.3    Wang, M.4    Stiegler, G.5
  • 4
    • 4544379899 scopus 로고    scopus 로고
    • Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope
    • Ofek G, Tang M, Sambor A, Katinger H, Mascola JR, et al. (2004) Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope. J Virol 78: 10724-10737.
    • (2004) J Virol , vol.78 , pp. 10724-10737
    • Ofek, G.1    Tang, M.2    Sambor, A.3    Katinger, H.4    Mascola, J.R.5
  • 5
    • 13844255333 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41
    • Cardoso RM, Zwick MB, Stanfield RL, Kunert R, Binley JM, et al. (2005) Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. Immunity 22: 163-173.
    • (2005) Immunity , vol.22 , pp. 163-173
    • Cardoso, R.M.1    Zwick, M.B.2    Stanfield, R.L.3    Kunert, R.4    Binley, J.M.5
  • 6
    • 21344434534 scopus 로고    scopus 로고
    • Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies
    • Haynes BF, Fleming J, St Clair EW, Katinger H, Stiegler G, et al. (2005) Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies. Science 308: 1906-1908.
    • (2005) Science , vol.308 , pp. 1906-1908
    • Haynes, B.F.1    Fleming, J.2    St Clair, E.W.3    Katinger, H.4    Stiegler, G.5
  • 7
    • 33947635198 scopus 로고    scopus 로고
    • The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes
    • Alam SM, McAdams M, Boren D, Rak M, Scearce RM, et al. (2007) The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes. J Immunol 178: 4424-4435.
    • (2007) J Immunol , vol.178 , pp. 4424-4435
    • Alam, S.M.1    McAdams, M.2    Boren, D.3    Rak, M.4    Scearce, R.M.5
  • 8
    • 73949133588 scopus 로고    scopus 로고
    • Role of HIV membrane in neutralization by two broadly neutralizing antibodies
    • Alam SM, Morelli M, Dennison SM, Liao HX, Zhang R, et al. (2009) Role of HIV membrane in neutralization by two broadly neutralizing antibodies. Proc Natl Acad Sci U S A 106: 20234-20239.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 20234-20239
    • Alam, S.M.1    Morelli, M.2    Dennison, S.M.3    Liao, H.X.4    Zhang, R.5
  • 9
    • 70349272203 scopus 로고    scopus 로고
    • Stable docking of neutralizing human immunodeficiency virus type 1 gp41 membrane-proximal external region monoclonal antibodies 2F5 and 4E10 is dependent on the membrane immersion depth of their epitope regions
    • Dennison SM, Stewart SM, Stempel KC, Liao HX, Haynes BF, et al. (2009) Stable docking of neutralizing human immunodeficiency virus type 1 gp41 membrane-proximal external region monoclonal antibodies 2F5 and 4E10 is dependent on the membrane immersion depth of their epitope regions. J Virol 83: 10211-10223.
    • (2009) J Virol , vol.83 , pp. 10211-10223
    • Dennison, S.M.1    Stewart, S.M.2    Stempel, K.C.3    Liao, H.X.4    Haynes, B.F.5
  • 10
    • 77649132440 scopus 로고    scopus 로고
    • Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region
    • Ofek G, McKee K, Yang Y, Yang ZY, Skinner J, et al. (2010) Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region. J Virol 84: 2955-2962.
    • (2010) J Virol , vol.84 , pp. 2955-2962
    • Ofek, G.1    McKee, K.2    Yang, Y.3    Yang, Z.Y.4    Skinner, J.5
  • 11
    • 76549125090 scopus 로고    scopus 로고
    • Aromatic residues at the edge of the antibody combining site facilitate viral glycoprotein recognition through membrane interactions
    • Scherer EM, Leaman DP, Zwick MB, McMichael AJ, Burton DR, (2010) Aromatic residues at the edge of the antibody combining site facilitate viral glycoprotein recognition through membrane interactions. Proc Natl Acad Sci U S A 107: 1529-1534.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 1529-1534
    • Scherer, E.M.1    Leaman, D.P.2    Zwick, M.B.3    McMichael, A.J.4    Burton, D.R.5
  • 12
    • 37849050487 scopus 로고    scopus 로고
    • HIV-1 hides an Achilles' heel in virion lipids
    • Haynes BF, Alam SM, (2008) HIV-1 hides an Achilles' heel in virion lipids. Immunity 28: 10-12.
    • (2008) Immunity , vol.28 , pp. 10-12
    • Haynes, B.F.1    Alam, S.M.2
  • 13
    • 76249083814 scopus 로고    scopus 로고
    • Autoreactivity in an HIV-1 broadly reactive neutralizing antibody variable region heavy chain induces immunologic tolerance
    • Verkoczy L, Diaz M, Holl TM, Ouyang YB, Bouton-Verville H, et al. (2010) Autoreactivity in an HIV-1 broadly reactive neutralizing antibody variable region heavy chain induces immunologic tolerance. Proc Natl Acad Sci U S A 107: 181-186.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 181-186
    • Verkoczy, L.1    Diaz, M.2    Holl, T.M.3    Ouyang, Y.B.4    Bouton-Verville, H.5
  • 14
    • 79651471386 scopus 로고    scopus 로고
    • Role of immunoglobulin light chain usage and MPER specificity in counterselecting B cells expressing the broadly neutralizing antibody 2F5
    • Abstract No. P04.55LB A-155
    • Verkoczy L, Bouton-Verville H, Hutchinson J, Scearce RM, Liao HX, et al. (2010) Role of immunoglobulin light chain usage and MPER specificity in counterselecting B cells expressing the broadly neutralizing antibody 2F5. AIDS Res Hum Retroviruses 26: Abstract No. P04.55LB A-155.
    • (2010) AIDS Res Hum Retroviruses , vol.26
    • Verkoczy, L.1    Bouton-Verville, H.2    Hutchinson, J.3    Scearce, R.M.4    Liao, H.X.5
  • 15
    • 41649090223 scopus 로고    scopus 로고
    • A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies
    • Frey G, Peng H, Rits-Volloch S, Morelli M, Cheng Y, et al. (2008) A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies. Proc Natl Acad Sci U S A 105: 3739-3744.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3739-3744
    • Frey, G.1    Peng, H.2    Rits-Volloch, S.3    Morelli, M.4    Cheng, Y.5
  • 16
    • 70449701456 scopus 로고    scopus 로고
    • Germline-like predecessors of broadly neutralizing antibodies lack measurable binding to HIV-1 envelope glycoproteins: implications for evasion of immune responses and design of vaccine immunogens
    • Xiao X, Chen W, Feng Y, Zhu Z, Prabakaran P, et al. (2009) Germline-like predecessors of broadly neutralizing antibodies lack measurable binding to HIV-1 envelope glycoproteins: implications for evasion of immune responses and design of vaccine immunogens. Biochem Biophys Res Commun 390: 404-409.
    • (2009) Biochem Biophys Res Commun , vol.390 , pp. 404-409
    • Xiao, X.1    Chen, W.2    Feng, Y.3    Zhu, Z.4    Prabakaran, P.5
  • 17
    • 77957198704 scopus 로고    scopus 로고
    • Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
    • Doores KJ, Burton DR, (2010) Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16. J Virol 84: 10510-10521.
    • (2010) J Virol , vol.84 , pp. 10510-10521
    • Doores, K.J.1    Burton, D.R.2
  • 18
    • 0031749469 scopus 로고    scopus 로고
    • A role for carbohydrates in immune evasion in AIDS
    • Reitter JN, Means RE, Desrosiers RC, (1998) A role for carbohydrates in immune evasion in AIDS. Nat Med 4: 679-684.
    • (1998) Nat Med , vol.4 , pp. 679-684
    • Reitter, J.N.1    Means, R.E.2    Desrosiers, R.C.3
  • 19
    • 0037389643 scopus 로고    scopus 로고
    • Rapid evolution of the neutralizing antibody response to HIV type 1 infection
    • Richman DD, Wrin T, Little SJ, Petropoulos CJ, (2003) Rapid evolution of the neutralizing antibody response to HIV type 1 infection. Proc Natl Acad Sci U S A 100: 4144-4149.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4144-4149
    • Richman, D.D.1    Wrin, T.2    Little, S.J.3    Petropoulos, C.J.4
  • 20
    • 17944380435 scopus 로고    scopus 로고
    • Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design
    • Saphire EO, Parren PW, Pantophlet R, Zwick MB, Morris GM, et al. (2001) Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design. Science 293: 1155-1159.
    • (2001) Science , vol.293 , pp. 1155-1159
    • Saphire, E.O.1    Parren, P.W.2    Pantophlet, R.3    Zwick, M.B.4    Morris, G.M.5
  • 21
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, Phogat SK, Chan-Hui PY, Wagner D, Phung P, et al. (2009) Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326: 285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1    Phogat, S.K.2    Chan-Hui, P.Y.3    Wagner, D.4    Phung, P.5
  • 22
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • Wei X, Decker JM, Wang S, Hui H, Kappes JC, et al. (2003) Antibody neutralization and escape by HIV-1. Nature 422: 307-312.
    • (2003) Nature , vol.422 , pp. 307-312
    • Wei, X.1    Decker, J.M.2    Wang, S.3    Hui, H.4    Kappes, J.C.5
  • 23
    • 57349148202 scopus 로고    scopus 로고
    • Glycosylation of gp41 of simian immunodeficiency virus shields epitopes that can be targets for neutralizing antibodies
    • Yuste E, Bixby J, Lifson J, Sato S, Johnson W, et al. (2008) Glycosylation of gp41 of simian immunodeficiency virus shields epitopes that can be targets for neutralizing antibodies. J Virol 82: 12472-12486.
    • (2008) J Virol , vol.82 , pp. 12472-12486
    • Yuste, E.1    Bixby, J.2    Lifson, J.3    Sato, S.4    Johnson, W.5
  • 24
    • 0345742562 scopus 로고    scopus 로고
    • Removal of N-linked glycosylation sites in the V1 region of simian immunodeficiency virus gp120 results in redirection of B-cell responses to V3
    • Cole KS, Steckbeck JD, Rowles JL, Desrosiers RC, Montelaro RC, (2004) Removal of N-linked glycosylation sites in the V1 region of simian immunodeficiency virus gp120 results in redirection of B-cell responses to V3. J Virol 78: 1525-1539.
    • (2004) J Virol , vol.78 , pp. 1525-1539
    • Cole, K.S.1    Steckbeck, J.D.2    Rowles, J.L.3    Desrosiers, R.C.4    Montelaro, R.C.5
  • 25
    • 1842562419 scopus 로고    scopus 로고
    • N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies
    • McCaffrey RA, Saunders C, Hensel M, Stamatatos L, (2004) N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies. J Virol 78: 3279-3295.
    • (2004) J Virol , vol.78 , pp. 3279-3295
    • McCaffrey, R.A.1    Saunders, C.2    Hensel, M.3    Stamatatos, L.4
  • 26
    • 77952561004 scopus 로고    scopus 로고
    • Deglycosylation of HIV-1 AE Gp140 enhances the capacity to elicit neutralizing antibodies against the heterologous HIV-1 clade
    • Zhang C, Wan Y, Shi J, Zhou M, Meng Z, et al. (2010) Deglycosylation of HIV-1 AE Gp140 enhances the capacity to elicit neutralizing antibodies against the heterologous HIV-1 clade. AIDS Res Hum Retroviruses 26: 569-575.
    • (2010) AIDS Res Hum Retroviruses , vol.26 , pp. 569-575
    • Zhang, C.1    Wan, Y.2    Shi, J.3    Zhou, M.4    Meng, Z.5
  • 27
    • 78349299783 scopus 로고    scopus 로고
    • Genetic signatures in the envelope glycoproteins of HIV-1 that associate with broadly neutralizing antibodies
    • Gnanakaran S, Daniels MG, Bhattacharya T, Lapedes AS, Sethi A, et al. (2010) Genetic signatures in the envelope glycoproteins of HIV-1 that associate with broadly neutralizing antibodies. PLoS Comput Biol 6: e1000955.
    • (2010) PLoS Comput Biol , vol.6
    • Gnanakaran, S.1    Daniels, M.G.2    Bhattacharya, T.3    Lapedes, A.S.4    Sethi, A.5
  • 28
    • 80053452683 scopus 로고    scopus 로고
    • Identification of amino acid substitutions associated with neutralization phenotype in the human immunodeficiency virus type-1 subtype C gp120
    • Virology
    • Kirchherr JL, Hamilton JW, Lu X, Gnanakaran S, Muldoon M, et al. (2010) Identification of amino acid substitutions associated with neutralization phenotype in the human immunodeficiency virus type-1 subtype C gp120. Virology pp. 1-12.
    • (2010) , pp. 1-12
    • Kirchherr, J.L.1    Hamilton, J.W.2    Lu, X.3    Gnanakaran, S.4    Muldoon, M.5
  • 29
    • 33746689169 scopus 로고    scopus 로고
    • Group M consensus Env oligomers induce antibodies that neutralize subtype C HIV- primary isolates
    • Liao HX, Sutherland LL, Xia SM, Brock ME, Scearce RM, et al. (2006) Group M consensus Env oligomers induce antibodies that neutralize subtype C HIV- primary isolates. Virology 353: 268-282.
    • (2006) Virology , vol.353 , pp. 268-282
    • Liao, H.X.1    Sutherland, L.L.2    Xia, S.M.3    Brock, M.E.4    Scearce, R.M.5
  • 30
    • 0035852822 scopus 로고    scopus 로고
    • Antibody 17b binding at the coreceptor site weakens the kinetics of the interaction of envelope glycoprotein gp120 with CD4
    • Zhang W, Godillot AP, Wyatt R, Sodroski J, Chaiken I, (2001) Antibody 17b binding at the coreceptor site weakens the kinetics of the interaction of envelope glycoprotein gp120 with CD4. Biochemistry 40: 1662-1670.
    • (2001) Biochemistry , vol.40 , pp. 1662-1670
    • Zhang, W.1    Godillot, A.P.2    Wyatt, R.3    Sodroski, J.4    Chaiken, I.5
  • 31
    • 0029119783 scopus 로고
    • Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding
    • Wyatt R, Moore J, Accola M, Desjardin E, Robinson J, et al. (1995) Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding. J Virol 69: 5723-5733.
    • (1995) J Virol , vol.69 , pp. 5723-5733
    • Wyatt, R.1    Moore, J.2    Accola, M.3    Desjardin, E.4    Robinson, J.5
  • 32
    • 70350134276 scopus 로고    scopus 로고
    • Cross-reactive monoclonal antibodies to multiple HIV-1 subtype and SIVcpz envelope glycoproteins
    • Gao F, Scearce RM, Alam SM, Hora B, Xia S, et al. (2009) Cross-reactive monoclonal antibodies to multiple HIV-1 subtype and SIVcpz envelope glycoproteins. Virology 394: 91-98.
    • (2009) Virology , vol.394 , pp. 91-98
    • Gao, F.1    Scearce, R.M.2    Alam, S.M.3    Hora, B.4    Xia, S.5
  • 33
    • 26444450696 scopus 로고    scopus 로고
    • Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12
    • Calarese DA, Lee HK, Huang CY, Best MD, Astronomo RD, et al. (2005) Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12. Proc Natl Acad Sci U S A 102: 13372-13377.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 13372-13377
    • Calarese, D.A.1    Lee, H.K.2    Huang, C.Y.3    Best, M.D.4    Astronomo, R.D.5
  • 34
    • 45549101708 scopus 로고    scopus 로고
    • Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility
    • Go EP, Irungu J, Zhang Y, Dalpathado DS, Liao HX, et al. (2008) Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility. J Proteome Res 7: 1660-1674.
    • (2008) J Proteome Res , vol.7 , pp. 1660-1674
    • Go, E.P.1    Irungu, J.2    Zhang, Y.3    Dalpathado, D.S.4    Liao, H.X.5
  • 35
    • 48349109797 scopus 로고    scopus 로고
    • Comparison of HPLC/ESI-FTICR MS versus MALDI-TOF/TOF MS for glycopeptide analysis of a highly glycosylated HIV envelope glycoprotein
    • Irungu J, Go EP, Zhang Y, Dalpathado DS, Liao HX, et al. (2008) Comparison of HPLC/ESI-FTICR MS versus MALDI-TOF/TOF MS for glycopeptide analysis of a highly glycosylated HIV envelope glycoprotein. J Am Soc Mass Spectrom 19: 1209-1220.
    • (2008) J Am Soc Mass Spectrom , vol.19 , pp. 1209-1220
    • Irungu, J.1    Go, E.P.2    Zhang, Y.3    Dalpathado, D.S.4    Liao, H.X.5
  • 37
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    • Sanders RW, Venturi M, Schiffner L, Kalyanaraman R, Katinger H, et al. (2002) The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J Virol 76: 7293-7305.
    • (2002) J Virol , vol.76 , pp. 7293-7305
    • Sanders, R.W.1    Venturi, M.2    Schiffner, L.3    Kalyanaraman, R.4    Katinger, H.5
  • 38
    • 33744937069 scopus 로고    scopus 로고
    • The HIV-neutralizing monoclonal antibody 4E10 recognizes N-terminal sequences on the native antigen
    • Hager-Braun C, Katinger H, Tomer KB, (2006) The HIV-neutralizing monoclonal antibody 4E10 recognizes N-terminal sequences on the native antigen. J Immunol 176: 7471-7481.
    • (2006) J Immunol , vol.176 , pp. 7471-7481
    • Hager-Braun, C.1    Katinger, H.2    Tomer, K.B.3
  • 39
    • 0036073140 scopus 로고    scopus 로고
    • Role of BCR affinity in T cell dependent antibody responses in vivo
    • Shih TA, Meffre E, Roederer M, Nussenzweig MC, (2002) Role of BCR affinity in T cell dependent antibody responses in vivo. Nat Immunol 3: 570-575.
    • (2002) Nat Immunol , vol.3 , pp. 570-575
    • Shih, T.A.1    Meffre, E.2    Roederer, M.3    Nussenzweig, M.C.4
  • 40
    • 0037029607 scopus 로고    scopus 로고
    • Very low affinity B cells form germinal centers, become memory B cells, and participate in secondary immune responses when higher affinity competition is reduced
    • Dal Porto J, Haberman A, Kelsoe G, Shlomchik M, (2002) Very low affinity B cells form germinal centers, become memory B cells, and participate in secondary immune responses when higher affinity competition is reduced. J Exp Med 195: 1215-1221.
    • (2002) J Exp Med , vol.195 , pp. 1215-1221
    • Dal Porto, J.1    Haberman, A.2    Kelsoe, G.3    Shlomchik, M.4
  • 41
    • 77951949737 scopus 로고    scopus 로고
    • SoDA2: a Hidden Markov Model approach for identification of immunoglobulin rearrangements
    • Munshaw S, Kepler TB, (2010) SoDA2: a Hidden Markov Model approach for identification of immunoglobulin rearrangements. Bioinformatics 26: 867-872.
    • (2010) Bioinformatics , vol.26 , pp. 867-872
    • Munshaw, S.1    Kepler, T.B.2
  • 42
    • 0019797407 scopus 로고
    • Evolutionary trees from DNA sequences: a maximum likelihood approach
    • Felsenstein J, (1981) Evolutionary trees from DNA sequences: a maximum likelihood approach. J Mol Evol 17: 368-376.
    • (1981) J Mol Evol , vol.17 , pp. 368-376
    • Felsenstein, J.1
  • 43
    • 0037311412 scopus 로고    scopus 로고
    • Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type 1 binding and neutralization by mannose-binding lectin
    • Hart ML, Saifuddin M, Spear GT, (2003) Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type 1 binding and neutralization by mannose-binding lectin. J Gen Virol 84: 353-360.
    • (2003) J Gen Virol , vol.84 , pp. 353-360
    • Hart, M.L.1    Saifuddin, M.2    Spear, G.T.3
  • 44
    • 41649109652 scopus 로고    scopus 로고
    • Targeting the carbohydrates on HIV-1: Interaction of oligomannose dendrons with human monoclonal antibody 2G12 and DC-SIGN
    • Wang SK, Liang PH, Astronomo RD, Hsu TL, Hsieh SL, et al. (2008) Targeting the carbohydrates on HIV-1: Interaction of oligomannose dendrons with human monoclonal antibody 2G12 and DC-SIGN. Proc Natl Acad Sci U S A 105: 3690-3695.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3690-3695
    • Wang, S.K.1    Liang, P.H.2    Astronomo, R.D.3    Hsu, T.L.4    Hsieh, S.L.5
  • 45
    • 77958115264 scopus 로고    scopus 로고
    • Limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals
    • Walker LM, Simek MD, Priddy F, Gach JS, Wagner D, et al. (2010) Limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals. PLoS Pathog 6 (8): e1001028.
    • (2010) PLoS Pathog , vol.6 , Issue.8
    • Walker, L.M.1    Simek, M.D.2    Priddy, F.3    Gach, J.S.4    Wagner, D.5
  • 46
    • 64049092486 scopus 로고    scopus 로고
    • In vivo gp41 antibodies targeting the 2F5 monoclonal antibody epitope mediate human immunodeficiency virus type 1 neutralization breadth
    • Shen X, Parks RJ, Montefiori DC, Kirchherr JL, Keele BF, et al. (2009) In vivo gp41 antibodies targeting the 2F5 monoclonal antibody epitope mediate human immunodeficiency virus type 1 neutralization breadth. J Virol 83: 3617-3625.
    • (2009) J Virol , vol.83 , pp. 3617-3625
    • Shen, X.1    Parks, R.J.2    Montefiori, D.C.3    Kirchherr, J.L.4    Keele, B.F.5
  • 47
    • 77950537428 scopus 로고    scopus 로고
    • Prolonged exposure of the HIV-1 gp41 membrane proximal region with L669S substitution
    • Shen X, Dennison SM, Liu P, Gao F, Jaeger F, et al. (2010) Prolonged exposure of the HIV-1 gp41 membrane proximal region with L669S substitution. Proc Natl Acad Sci U S A 107: 5972-5977.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5972-5977
    • Shen, X.1    Dennison, S.M.2    Liu, P.3    Gao, F.4    Jaeger, F.5
  • 48
    • 38849205377 scopus 로고    scopus 로고
    • Enhancing exposure of HIV-1 neutralization epitopes through mutations in gp41
    • Blish CA, Nguyen MA, Overbaugh J, (2008) Enhancing exposure of HIV-1 neutralization epitopes through mutations in gp41. PLoS Med 5 (1): e9.
    • (2008) PLoS Med , vol.5 , Issue.1
    • Blish, C.A.1    Nguyen, M.A.2    Overbaugh, J.3
  • 49
    • 0026533764 scopus 로고
    • Influence of carbohydrate moieties on the immunogenicity of human immunodeficiency virus type 1 recombinant gp160
    • Benjouad A, Gluckman JC, Rochat H, Montagnier L, Bahraoui E, (1992) Influence of carbohydrate moieties on the immunogenicity of human immunodeficiency virus type 1 recombinant gp160. J Virol 66: 2473-2483.
    • (1992) J Virol , vol.66 , pp. 2473-2483
    • Benjouad, A.1    Gluckman, J.C.2    Rochat, H.3    Montagnier, L.4    Bahraoui, E.5
  • 50
    • 77956247505 scopus 로고    scopus 로고
    • Design of a non-glycosylated outer domain-derived HIV-1 gp120 immunogen that binds to CD4 and induces neutralizing antibodies
    • Bhattacharyya S, Rajan RE, Swarupa Y, Rathore U, Verma A, et al. (2010) Design of a non-glycosylated outer domain-derived HIV-1 gp120 immunogen that binds to CD4 and induces neutralizing antibodies. J Biol Chem 285: 27100-27110.
    • (2010) J Biol Chem , vol.285 , pp. 27100-27110
    • Bhattacharyya, S.1    Rajan, R.E.2    Swarupa, Y.3    Rathore, U.4    Verma, A.5
  • 51
    • 77952001983 scopus 로고    scopus 로고
    • Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization
    • Binley JM, Ban YE, Crooks ET, Eggink D, Osawa K, et al. (2010) Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization. J Virol 84: 5637-5655.
    • (2010) J Virol , vol.84 , pp. 5637-5655
    • Binley, J.M.1    Ban, Y.E.2    Crooks, E.T.3    Eggink, D.4    Osawa, K.5
  • 52
    • 0032501955 scopus 로고    scopus 로고
    • Analysis of the interaction of antibodies with a conserved enzymatically deglycosylated core of the HIV type 1 envelope glycoprotein 120
    • Binley JM, Wyatt R, Desjardins E, Kwong PD, Hendrickson W, et al. (1998) Analysis of the interaction of antibodies with a conserved enzymatically deglycosylated core of the HIV type 1 envelope glycoprotein 120. AIDS Res Hum Retroviruses 14: 191-198.
    • (1998) AIDS Res Hum Retroviruses , vol.14 , pp. 191-198
    • Binley, J.M.1    Wyatt, R.2    Desjardins, E.3    Kwong, P.D.4    Hendrickson, W.5
  • 53
    • 0041920924 scopus 로고    scopus 로고
    • Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition
    • Koch M, Pancera M, Kwong PD, Kolchinsky P, Grundner C, et al. (2003) Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition. Virology 313: 387-400.
    • (2003) Virology , vol.313 , pp. 387-400
    • Koch, M.1    Pancera, M.2    Kwong, P.D.3    Kolchinsky, P.4    Grundner, C.5
  • 54
    • 33748925430 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity
    • Sagar M, Wu X, Lee S, Overbaugh J, (2006) Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity. J Virol 80: 9586-9598.
    • (2006) J Virol , vol.80 , pp. 9586-9598
    • Sagar, M.1    Wu, X.2    Lee, S.3    Overbaugh, J.4
  • 55
    • 77957271989 scopus 로고    scopus 로고
    • Expression-system-dependent modulation of HIV-1 envelope glycoprotein antigenicity and immunogenicity
    • Kong L, Sheppard NC, Stewart-Jones GB, Robson CL, Chen H, et al. (2010) Expression-system-dependent modulation of HIV-1 envelope glycoprotein antigenicity and immunogenicity. J Mol Biol 403: 131-147.
    • (2010) J Mol Biol , vol.403 , pp. 131-147
    • Kong, L.1    Sheppard, N.C.2    Stewart-Jones, G.B.3    Robson, C.L.4    Chen, H.5
  • 57
    • 70449464779 scopus 로고    scopus 로고
    • Activating systemic autoimmunity: B's, T's, and tolls
    • Shlomchik MJ, (2009) Activating systemic autoimmunity: B's, T's, and tolls. Curr Opin Immunol 21: 626-633.
    • (2009) Curr Opin Immunol , vol.21 , pp. 626-633
    • Shlomchik, M.J.1
  • 58
    • 0036101339 scopus 로고    scopus 로고
    • Functional evaluation of DC-SIGN monoclonal antibodies reveals DC-SIGN interactions with ICAM-3 do not promote human immunodeficiency virus type 1 transmission
    • Wu L, Martin TD, Vazeux R, Unutmaz D, KewalRamani VN, (2002) Functional evaluation of DC-SIGN monoclonal antibodies reveals DC-SIGN interactions with ICAM-3 do not promote human immunodeficiency virus type 1 transmission. J Virol 76: 5905-5914.
    • (2002) J Virol , vol.76 , pp. 5905-5914
    • Wu, L.1    Martin, T.D.2    Vazeux, R.3    Unutmaz, D.4    KewalRamani, V.N.5
  • 59
  • 60


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